SOLID-STATE NMR ANALYSIS OF CROSS-LINKING IN MUSSEL PROTEIN GLUE

被引：43

作者：

HOLL, SM

HANSEN, D

WAITE, JH

SCHAEFER, J

机构：

[1] WASHINGTON UNIV,DEPT CHEM,ST LOUIS,MO 63130

[2] UNIV DELAWARE,COLL MARINE STUDIES,LEWES,DE 19958

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1993年 / 302卷 / 01期

关键词：

D O I：

10.1006/abbi.1993.1207

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Solid-state 13C and 15N NMR spectra have been obtained of intact adhesive plaques from the mussel Geukensia demissa labeled by L-[6-13C,6-15N]lysine. The plaques are rich in a polyphenolic protein glue which has 50 or more repeats of a nonapeptide sequence with one lysine per repeat. The average isotopic 15N enrichment of lysyl ε{lunate} nitrogens in the plaques was 4%. These lysyl amines are not involved in ionic complexes and do not form observable concentrations of covalent crosslinks. © 1993 Academic Press. All rights reserved.

引用

页码：255 / 258

页数：4

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